Comparative Proteomics Analysis of Cerebrospinal Fluid of Patients with Guillain–Barré Syndrome

• Published in: Cellular and molecular neurobiology Vol. 28; no. 5; pp. 737 - 744
• Main Authors: Yang, Yin-Rong, Liu, Shi-Lian, Qin, Zhao-Yu, Liu, Fu-Jun, Qin, Yan-Jiang, Bai, Shu-Mei, Chen, Zhe-Yu
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01.08.2008
• Subjects: Adolescent; Adult; alpha 1-Antitrypsin - analysis; alpha 1-Antitrypsin - cerebrospinal fluid; Apolipoproteins A - analysis; Apolipoproteins A - cerebrospinal fluid; Biomarkers - analysis; Biomarkers - cerebrospinal fluid; Biomedical and Life Sciences; Biomedicine; Cell Biology; Cerebrospinal Fluid Proteins - analysis; Electrophoresis, Gel, Two-Dimensional; Enzyme-Linked Immunosorbent Assay; Female; Guillain-Barre Syndrome - cerebrospinal fluid; Guillain-Barre Syndrome - diagnosis; Guillain-Barre Syndrome - physiopathology; Haptoglobins - analysis; Haptoglobins - cerebrospinal fluid; Humans; Male; Mass Spectrometry; Middle Aged; Neurobiology; Neurofilament Proteins - analysis; Neurofilament Proteins - cerebrospinal fluid; Neurosciences; Original Paper; Predictive Value of Tests; Proteomics - methods; Guillain–Barré syndrome; Proteome; Cerebrospinal fluid; Two-dimensional electrophoresis; Mass Spectrometry; ELISA
• ISSN: 0272-4340; 1573-6830
• DOI: 10.1007/s10571-007-9257-7

To better understand the pathophysiologic mechanisms underlying Guillain–Barré syndrome (GBS), Comparative proteomic analysis of cerebrospinal fluid (CSF) between patients with GBS (the experiment group) and control subjects suffering from other neurological disorders (the control group) was carried out using two-dimensional gel electrophoresis (2-DE) technique, in combination with matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF MS) and database searching to determine abnormal CSF proteins in GBS patients. Image analysis of 2-DE gels silver stained revealed that 10 protein spots showed significant differential expression between the two groups of CSF samples. The expression of cystatin C, transthyretin, apolipoprotein E and heat shock protein 70 were decreased. However, haptoglobin, α-1-antitrypsin, apolipoprotein A-IV and neurofilaments were elevated. The subsequent ELISA measured the concentration of cystatin C and confirmed the result of the proteomic analysis. These identified proteins may be involved in the pathophysiological process of GBS and call for further studying the role of these proteins in the pathogenesis of the disease.